Highly conserved configuration of catalytic amino acid residues among calicivirus-encoded proteases

被引:22
作者
Oka, Tomoichiro
Yamamoto, Mami
Yokoyama, Masaru
Ogawa, Satoko
Hansman, Grant S.
Katayama, Kazuhiko
Miyashita, Kana
Takagi, Hirotaka
Tohya, Yukinobu
Sato, Hironori
Takeda, Naokazu
机构
[1] Natl Inst Infect Dis, Dept Virol 2, Musashino, Tokyo 2080011, Japan
[2] Natl Inst Infect Dis, Ctr Pathogen Genom, Musashino, Tokyo 2080011, Japan
[3] Natl Inst Infect Dis, Div Biosafety Control & Res, Shinjuku Ku, Tokyo 1628640, Japan
[4] Univ Tokyo, Dept Vet Microbiol, Grad Sch Agr & Life Sci, Bunkyo Ku, Tokyo 1138657, Japan
关键词
D O I
10.1128/JVI.02840-06
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A common feature of caliciviruses is the proteolytic processing of the viral polyprotein catalyzed by the viral 3C-like protease encoded in open reading frame 1 (ORF1). Here we report the identification and structural characterization of the protease domains and amino acid residues in sapovirus (SaV) and feline calicivirus (FCV). The in vitro expression and processing of a panel of truncated ORF1 polyproteins and corresponding mutant forms showed that the functional protease domain is 146 amino acids (aa) in SaV and 154 aa in FCV. Site-directed 52 mutagenesis of the protease domains identified four amino acid residues essential to protease activities: W, E, C-116, and H-131 in SaV and H-39, E-60, C-122, and H-137 in FCV. A computer-assisted structural analysis showed that despite high levels of diversity in the primary structures of the protease domains in the family Caliciviridae, the configurations of the H, E, C, and H residues are highly conserved, with these residues positioned closely along the inner surface of the potential binding cleft for the substrate. These results strongly suggest that the H, E, C, and H residues are involved in the formation of a conserved catalytic surface of the SaV and FCV 3C-like proteases.
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页码:6798 / 6806
页数:9
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